ANPRC_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: ANPRC_HUMAN
• UniProt AC: P17342
• Protein Name: Atrial natriuretic peptide receptor 3
• Gene Name: NPR3
• Organism: Homo sapiens (Human).
• Sequence Length: 541
• Subcellular Localization: Membrane; Single-pass type I membrane protein.
• Protein Description: Receptor for the natriuretic peptide hormones, binding with similar affinities atrial natriuretic peptide NPPA/ANP, brain natriuretic peptide NPPB/BNP, and C-type natriuretic peptide NPPC/CNP. May function as a clearance receptor for NPPA, NPPB and NPPC, regulating their local concentrations and effects. May regulate diuresis, blood pressure and skeletal development. Does not have guanylate cyclase activity..
• Protein Sequence: MPSLLVLTFSPCVLLGWALLAGGTGGGGVGGGGGGAGIGGGRQEREALPPQKIEVLVLLPQDDSYLFSLTRVRPAIEYALRSVEGNGTGRRLLPPGTRFQVAYEDSDCGNRALFSLVDRVAAARGAKPDLILGPVCEYAAAPVARLASHWDLPMLSAGALAAGFQHKDSEYSHLTRVAPAYAKMGEMMLALFRHHHWSRAALVYSDDKLERNCYFTLEGVHEVFQEEGLHTSIYSFDETKDLDLEDIVRNIQASERVVIMCASSDTIRSIMLVAHRHGMTSGDYAFFNIELFNSSSYGDGSWKRGDKHDFEAKQAYSSLQTVTLLRTVKPEFEKFSMEVKSSVEKQGLNMEDYVNMFVEGFHDAILLYVLALHEVLRAGYSKKDGGKIIQQTWNRTFEGIAGQVSIDANGDRYGDFSVIAMTDVEAGTQEVIGDYFGKEGRFEMRPNVKYPWGPLKLRIDENRIVEHTNSSPCKSSGGLEESAVTGIVVGALLGAGLLMAFYFFRKKYRITIERRTQQEESNLGKHRELREDSIRSHFSVA

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
78	Phosphorylation	RVRPAIEYALRSVEG EHHHHHHHHHHHCCC	12.57	22468782
82	Phosphorylation	AIEYALRSVEGNGTG HHHHHHHHCCCCCCC	25.93	22468782
86	N-linked_Glycosylation	ALRSVEGNGTGRRLL HHHHCCCCCCCCCCC	31.20	16870210
86	N-linked_Glycosylation	ALRSVEGNGTGRRLL HHHHCCCCCCCCCCC	31.20	16870210
148	Phosphorylation	APVARLASHWDLPML HHHHHHHHCCCCCCC	29.69	46164525
156	Phosphorylation	HWDLPMLSAGALAAG CCCCCCCCHHHHHHC	20.57	46164531
293	N-linked_Glycosylation	FFNIELFNSSSYGDG EEEEEEECCCCCCCC	54.31	11533490
293	N-linked_Glycosylation	FFNIELFNSSSYGDG EEEEEEECCCCCCCC	54.31	11533490
316	Phosphorylation	DFEAKQAYSSLQTVT CHHHHHHHHHHHHHH	9.04	7322779
353	Phosphorylation	QGLNMEDYVNMFVEG CCCCHHHHHHHHHHH	4.76	24043423
368	Phosphorylation	FHDAILLYVLALHEV HHHHHHHHHHHHHHH	7.03	24043423
392	O-linked_Glycosylation	GGKIIQQTWNRTFEG CCCEEHHHCCCCCCC	14.34	30620550
394	N-linked_Glycosylation	KIIQQTWNRTFEGIA CEEHHHCCCCCCCCC	36.18	11533490
394	N-linked_Glycosylation	KIIQQTWNRTFEGIA CEEHHHCCCCCCCCC	36.18	11533490
456	Ubiquitination	KYPWGPLKLRIDENR CCCCCCCEEEECCCC	38.56	-
502	Phosphorylation	AGLLMAFYFFRKKYR HHHHHHHHHHHHHHC	7.71	72839137
524 (in isoform 2)	Ubiquitination	-	28.16	-
525	Ubiquitination	QEESNLGKHRELRED HHHHCCCCCHHHHHH	42.53	-
532	Phosphorylation	KHRELREDSIRSHFS CCHHHHHHHHHHHCC	42.82	24719451
533	Phosphorylation	HRELREDSIRSHFSV CHHHHHHHHHHHCCC	18.36	26055452
536	Phosphorylation	LREDSIRSHFSVA-- HHHHHHHHHCCCC--	27.49	26425664
539	Phosphorylation	DSIRSHFSVA----- HHHHHHCCCC-----	16.23	26055452

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Oops, there are no upstream regulatory protein records of ANPRC_HUMAN !!

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of ANPRC_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of ANPRC_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANF_HUMAN	NPPA	physical	1309330
ANFB_HUMAN	NPPB	physical	1309330
ANFC_HUMAN	NPPC	physical	1309330
ANF_HUMAN	NPPA	physical	1660465
ANFB_HUMAN	NPPB	physical	1660465
ANFC_HUMAN	NPPC	physical	1660465
ANFB_HUMAN	NPPB	physical	1672777
ANFC_HUMAN	NPPC	physical	1672777
ANF_HUMAN	NPPA	physical	1672777

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.

Related Literatures of Post-Translational Modification

N-linked Glycosylation

"Structural determinants of natriuretic peptide receptor specificityand degeneracy.";
He X.-L., Dukkipati A., Garcia K.C.;
J. Mol. Biol. 361:698-714(2006).
Cited for: X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-480 IN COMPLEX WITHNATRIURETIC PEPTIDE AND CHLORIDE IONS, GLYCOSYLATION AT ASN-86;ASN-293 AND ASN-394, AND DISULFIDE BONDS.
PubMed: 16870210

"Allosteric activation of a spring-loaded natriuretic peptide receptordimer by hormone.";
He X.-L., Chow D.-C., Martick M.M., Garcia K.C.;
Science 293:1657-1662(2001).
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 44-485 IN COMPLEX WITHNATRIURETIC PEPTIDE, GLYCOSYLATION AT ASN-293 AND ASN-394, DISULFIDEBONDS, AND SUBUNIT.
PubMed: 11533490

"The disulfide linkages and glycosylation sites of the humannatriuretic peptide receptor-C homodimer.";
Stults J.T., O'Connell K.L., Garcia C., Wong S., Engel A.M.,Garbers D.L., Lowe D.G.;
Biochemistry 33:11372-11381(1994).
Cited for: PARTIAL PROTEIN SEQUENCE (ISOFORMS 1 AND 2), DISULFIDE BONDS,GLYCOSYLATION AT ASN-86; ASN-293 AND ASN-394, AND STRUCTURE OFCARBOHYDRATES.
PubMed: 7727388

Phosphorylation

"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-533, AND MASSSPECTROMETRY.
PubMed: 17081983